Abstract
(1) A ( K + + H + )- ATPase containing membrane fraction, isolated from pig gastric mucosa, has been further purified by means of zonal electrophoresis, leading to a 20% increase in specific activity and an increase in ratio of ( K + + H + )- ATPase to basal Mg 2+-ATPase activity from 9 to 20. (2) The target size of ( Na + + K + )- ATPase , determined by radiation inactivation analysis, is 332 kDa, in excellent agreement with the earlier value of 327 kDa obtained from the subunit composition and subunit molecular weights. This shows that the Kepner-Macey factor of 6.4·10 11 is valid for membrane-bound ATPases. (3) The target size of ( K + + H + )- ATPase is 444 kDa, which, in connection with a subunit molecular weight of 110000, suggests a tetrameric assembly of the native enzyme. The ouabain-insensitive K +-stimulated p- nitrophenylphosphatase activity has a target size of 295 kDa. (4) In the presence of added Mg 2+ the target sizes of the ( K + + H + )- ATPase and its phosphatase activity are decreased by about 15%, while that for the ( Na + + K + )- ATPase is not significantly changed. This observation is discussed in terms of a Mg 2+-induced tightening of the subunits composing the ( K + + H + )- ATPase molecule.
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